Tris-sucrose buffer system: a new specially designed medium for extracellular invertase production by immobilized cells of isolated yeast Cryptococcus laurentii MT-61
Language English Country United States Media print-electronic
Document type Journal Article
- MeSH
- Biotechnology methods MeSH
- Time Factors MeSH
- Cryptococcus enzymology metabolism MeSH
- Cells, Immobilized enzymology metabolism MeSH
- beta-Fructofuranosidase isolation & purification MeSH
- Hydrogen-Ion Concentration MeSH
- Culture Media chemistry MeSH
- Buffers MeSH
- Sucrose MeSH
- Temperature MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- beta-Fructofuranosidase MeSH
- Culture Media MeSH
- Buffers MeSH
- Sucrose MeSH
The aims of the present study were to isolate new yeasts with high extracellular (exo) invertase activity and to investigate the usability of buffer systems as invertase production media by immobilized yeast cells. Among 70 yeast isolates, Cryptococcus laurentii MT-61 had the highest exo-invertase activity. Immobilization of yeast cells was performed using sodium alginate. Higher exo-invertase activity for immobilized cells was achieved in tris-sucrose buffer system (TSBS) compared to sodium acetate buffer system and potassium phosphate buffer system. TSBS was prepared by dissolving 30 g of sucrose in 1 L of tris buffer solution. The optimum pH, temperature, and incubation time for invertase production with immobilized cells were determined as 8.0, 35 °C and 36 h in TSBS, respectively. Under optimized conditions, maximum exo-invertase activity was found to be 28.4 U/mL in sterile and nonsterile TSBS. Immobilized cells could be reused in 14 and 12 successive cycles in sterile and nonsterile TSBS without any loss in the maximum invertase activity, respectively. This is the first report which showed that immobilized microbial cells could be used as a biocatalyst for exo-invertase production in buffer system. As an additional contribution, a new yeast strain with high invertase activity was isolated.
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